[35-S]sulfate incorporation into myelin clycoproteins; II. Peripheral nervous tissue

Abstract

The in vivo incorporation of [35-S]sulfate, [3-H]fucose and [3-H]leucine into sciatic nerve myelin was investigatedmpolyacrylamide gel electrophoresis of thr proteins indicated that the 35-S-labeling of proteins occurred almost exclusively in the major myelin protein; A smaller myelin glycoprotein migrating just ahead of the major one was labeled with [3-H]fucose but did not incorporate 35-S to a detectable extent. There was little or no 35-S associated with basic proteins on polyacrylamide gels when the proteins were extracted with chloroform/methanol; Fucose-labeled myelin glycoproteins were converted to glycopeptides by pronase digestion; The glycopeptides gave a single peak on tsephadex G-50 in which the 3-H and 35-S coincided. The association of 35-S with glycopeptides was not caused by binding of sulfatide or free inorganic sulfate. This study shows that the major myelin protein in the sciatic nerve of the rat is glycosylated and sulfated.